TAAR2_HUMAN
ID TAAR2_HUMAN Reviewed; 351 AA.
AC Q9P1P5; Q5QD02; Q6NWS1; Q6NWS2; Q6NWS3;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 2.
DT 03-AUG-2022, entry version 159.
DE RecName: Full=Trace amine-associated receptor 2;
DE Short=TaR-2;
DE Short=Trace amine receptor 2;
DE AltName: Full=G-protein coupled receptor 58;
GN Name=TAAR2; Synonyms=GPR58;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=10684976; DOI=10.1016/s0167-4781(99)00241-9;
RA Lee D.K., Lynch K.R., Nguyen T., Im D.-S., Cheng R., Saldivia V.R., Liu Y.,
RA Liu I.S.C., Heng H.H.Q., Seeman P., George S.R., O'Dowd B.F., Marchese A.;
RT "Cloning and characterization of additional members of the G protein-
RT coupled receptor family.";
RL Biochim. Biophys. Acta 1490:311-323(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=15718104; DOI=10.1016/j.ygeno.2004.11.010;
RA Lindemann L., Ebeling M., Kratochwil N.A., Bunzow J.R., Grandy D.K.,
RA Hoener M.C.;
RT "Trace amine-associated receptors form structurally and functionally
RT distinct subfamilies of novel G protein-coupled receptors.";
RL Genomics 85:372-385(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
CC -!- FUNCTION: Orphan receptor.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=Long;
CC IsoId=Q9P1P5-1; Sequence=Displayed;
CC Name=2; Synonyms=Small;
CC IsoId=Q9P1P5-2; Sequence=VSP_016301;
CC -!- TISSUE SPECIFICITY: Not expressed in the pons, thalamus, hypothalamus,
CC hippocampus, caudate, putamen, frontal cortex, basal forebrain,
CC midbrain or liver.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; AF112460; AAF27278.1; -; Genomic_DNA.
DR EMBL; AY703480; AAV70150.1; -; mRNA.
DR EMBL; AY702304; AAV70122.1; -; mRNA.
DR EMBL; AL513524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC067461; AAH67461.1; -; mRNA.
DR EMBL; BC067462; AAH67462.1; -; mRNA.
DR EMBL; BC067463; AAH67463.1; -; mRNA.
DR CCDS; CCDS34541.1; -. [Q9P1P5-1]
DR CCDS; CCDS5157.1; -. [Q9P1P5-2]
DR RefSeq; NP_001028252.1; NM_001033080.1. [Q9P1P5-1]
DR RefSeq; NP_055441.2; NM_014626.3. [Q9P1P5-2]
DR AlphaFoldDB; Q9P1P5; -.
DR SMR; Q9P1P5; -.
DR BioGRID; 114702; 4.
DR STRING; 9606.ENSP00000356908; -.
DR ChEMBL; CHEMBL4523927; -.
DR GlyGen; Q9P1P5; 3 sites.
DR iPTMnet; Q9P1P5; -.
DR PhosphoSitePlus; Q9P1P5; -.
DR BioMuta; TAAR2; -.
DR DMDM; 82592527; -.
DR PaxDb; Q9P1P5; -.
DR PRIDE; Q9P1P5; -.
DR Antibodypedia; 19711; 105 antibodies from 25 providers.
DR DNASU; 9287; -.
DR Ensembl; ENST00000275191.2; ENSP00000275191.2; ENSG00000146378.6. [Q9P1P5-2]
DR Ensembl; ENST00000367931.1; ENSP00000356908.1; ENSG00000146378.6. [Q9P1P5-1]
DR GeneID; 9287; -.
DR KEGG; hsa:9287; -.
DR MANE-Select; ENST00000367931.1; ENSP00000356908.1; NM_001033080.1; NP_001028252.1.
DR UCSC; uc003qdl.1; human. [Q9P1P5-1]
DR CTD; 9287; -.
DR DisGeNET; 9287; -.
DR GeneCards; TAAR2; -.
DR HGNC; HGNC:4514; TAAR2.
DR HPA; ENSG00000146378; Not detected.
DR MIM; 604849; gene.
DR neXtProt; NX_Q9P1P5; -.
DR OpenTargets; ENSG00000146378; -.
DR PharmGKB; PA28903; -.
DR VEuPathDB; HostDB:ENSG00000146378; -.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT00940000161475; -.
DR HOGENOM; CLU_009579_11_0_1; -.
DR InParanoid; Q9P1P5; -.
DR OMA; DCSEFGN; -.
DR OrthoDB; 913195at2759; -.
DR PhylomeDB; Q9P1P5; -.
DR TreeFam; TF343107; -.
DR PathwayCommons; Q9P1P5; -.
DR Reactome; R-HSA-375280; Amine ligand-binding receptors.
DR Reactome; R-HSA-418555; G alpha (s) signalling events.
DR Reactome; R-HSA-9660821; ADORA2B mediated anti-inflammatory cytokines production.
DR BioGRID-ORCS; 9287; 7 hits in 1060 CRISPR screens.
DR GeneWiki; TAAR2; -.
DR GenomeRNAi; 9287; -.
DR Pharos; Q9P1P5; Tbio.
DR PRO; PR:Q9P1P5; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9P1P5; protein.
DR Bgee; ENSG00000146378; Expressed in tibialis anterior and 6 other tissues.
DR Genevisible; Q9P1P5; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004930; F:G protein-coupled receptor activity; TAS:ProtInc.
DR GO; GO:0001594; F:trace-amine receptor activity; IBA:GO_Central.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; TAS:GDB.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR InterPro; IPR009132; TAAR_fam.
DR Pfam; PF00001; 7tm_1; 1.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PRINTS; PR01830; TRACEAMINER.
DR SMART; SM01381; 7TM_GPCR_Srsx; 1.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cell membrane; Disulfide bond;
KW G-protein coupled receptor; Glycoprotein; Membrane; Receptor;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..351
FT /note="Trace amine-associated receptor 2"
FT /id="PRO_0000070146"
FT TOPO_DOM 1..48
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical; Name=1"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..79
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 80..100
FT /note="Helical; Name=2"
FT /evidence="ECO:0000255"
FT TOPO_DOM 101..118
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 119..139
FT /note="Helical; Name=3"
FT /evidence="ECO:0000255"
FT TOPO_DOM 140..162
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical; Name=4"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..207
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 208..228
FT /note="Helical; Name=5"
FT /evidence="ECO:0000255"
FT TOPO_DOM 229..263
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 264..284
FT /note="Helical; Name=6"
FT /evidence="ECO:0000255"
FT TOPO_DOM 285..299
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 300..322
FT /note="Helical; Name=7"
FT /evidence="ECO:0000255"
FT TOPO_DOM 323..351
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 24
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 289
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 116..201
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT VAR_SEQ 1..45
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:15718104"
FT /id="VSP_016301"
FT CONFLICT 178
FT /note="V -> A (in Ref. 1; AAF27278)"
FT /evidence="ECO:0000305"
FT CONFLICT 301
FT /note="T -> K (in Ref. 4; AAH67463)"
FT /evidence="ECO:0000305"
FT CONFLICT 329
FT /note="I -> V (in Ref. 4; AAH67462)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 351 AA; 40134 MW; 7AA0BAAC58E2F11D CRC64;
MAVSSEQHEL SHFKRTQTKK EKFNCSEYGN RSCPENERSL GVRVAMYSFM AGSIFITIFG
NLAMIISISY FKQLHTPTNF LILSMAITDF LLGFTIMPYS MIRSVENCWY FGLTFCKIYY
SFDLMLSITS IFHLCSVAID RFYAICYPLL YSTKITIPVI KRLLLLCWSV PGAFAFGVVF
SEAYADGIEG YDILVACSSS CPVMFNKLWG TTLFMAGFFT PGSMMVGIYG KIFAVSRKHA
HAINNLRENQ NNQVKKDKKA AKTLGIVIGV FLLCWFPCFF TILLDPFLNF STPVVLFDAL
TWFGYFNSTC NPLIYGFFYP WFRRALKYIL LGKIFSSCFH NTILCMQKES E
